Hydrodynamic trapping measures the interaction between membrane-associated molecules
Autor: | Ana Filipa L.O.M. Santos, Jana Hladilkova, Peter Jönsson, Victoria Junghans, Simon J. Davis, Mikael Lund |
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Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Streptavidin Flexibility (anatomy) Glycosylation Lipid Bilayers CD2 Antigens lcsh:Medicine 02 engineering and technology 010402 general chemistry Hydrodynamic trapping 01 natural sciences Article 03 medical and health sciences chemistry.chemical_compound Membrane associated medicine Molecule Humans Lipid bilayer lcsh:Science 030304 developmental biology 0303 health sciences Multidisciplinary Membranes Chemistry lcsh:R Membrane Proteins 021001 nanoscience & nanotechnology 0104 chemical sciences 030104 developmental biology medicine.anatomical_structure Membrane protein CD4 Antigens Biophysics Hydrodynamics Leukocyte Common Antigens lcsh:Q 0210 nano-technology |
Zdroj: | Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018) Scientific Reports |
ISSN: | 2045-2322 |
DOI: | 10.1038/s41598-018-30285-0 |
Popis: | How membrane proteins distribute and behave on the surface of cells is determined by the molecules’ interaction potential. However, measuring this potential, and how it varies with protein-to-protein distance, has been challenging. We here present how a method we call hydrodynamic trapping can achieve this. Our method uses the focused liquid flow from a micropipette to locally accumulate molecules protruding from a lipid membrane. The interaction potential, as well as information about the dimensions of the studied molecule, are obtained by relating the degree of accumulation to the strength of the trap. We have used this to study four representative proteins, with different height-to-width ratios and protein properties; from the globular streptavidin, to the rod-like immune cell proteins CD2, CD4 and CD45. The obtained data illustrates how protein shape, glycosylation and flexibility influence the behaviour of membrane proteins as well as underline the general applicability of the method. |
Databáze: | OpenAIRE |
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